Identification and characterization of acidic hydrolases with chitinase and chitosanase activities from sweet orange callus tissue.
Identifieur interne : 000E81 ( PubMed/Checkpoint ); précédent : 000E80; suivant : 000E82Identification and characterization of acidic hydrolases with chitinase and chitosanase activities from sweet orange callus tissue.
Auteurs : W F Osswald [États-Unis] ; J P Shapiro ; H. Doostdar ; R E Mcdonald ; R P Niedz ; C J Nairn ; C J Hearn ; R T MayerSource :
- Plant & cell physiology [ 0032-0781 ] ; 1994.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Chitinase, Glycoside Hydrolases.
- chemical , isolation & purification : Chitinase, Glycoside Hydrolases.
- enzymology : Citrus.
- genetics : Citrus.
- Amino Acid Sequence, Isoelectric Point, Molecular Sequence Data, Molecular Weight, Sequence Homology, Amino Acid.
Abstract
Acidic chitinases (EC 3.2.1.14) were isolated and characterized from 4-week-old nonembryogenic Citrus sinensis L. Osbeck cv 'Valencia' callus tissue. The enzymes were purified using size exclusion, anion exchange, and chromatofocusing HPLC techniques. Eleven isoforms were isolated with M(r)s between 26,000 and 37,400. Eight of the isoforms were purified to homogeneity, and all but one cross-reacted with a polyclonal antibody raised against a basic class I potato leaf chitinase. The isoelectric points (determined by chromatofocusing) were from pH 4.5 to 5.4. All hydrolases degraded chitin and four were capable of hydrolyzing solubilized shrimp shell chitosan suggesting they may be chitosanases (EC 3.2.1.99). Apparent chitosanase activity generally decreased with decreasing acetylation of the chitosan (i.e. from 20% to 0% acetylation). The chitinases and chitinases/chitosanases are predominantly endochitinases. Chitosanase activity was optimal at pH 5 while the pH optimum for chitinase activity ranged between pH 3.5 and 5.5. The chitinases and chitinases/chitosanases were stable up to 60 degrees C and showed their highest enzyme activity at that temperature. N-terminal sequences were obtained on three of the isoforms. One of the isoforms was identified as a class II chitinase and the other two as class III chitinases.
PubMed: 7952962
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Identification and characterization of acidic hydrolases with chitinase and chitosanase activities from sweet orange callus tissue.</title><author><name sortKey="Osswald, W F" sort="Osswald, W F" uniqKey="Osswald W" first="W F" last="Osswald">W F Osswald</name><affiliation wicri:level="2"><nlm:affiliation>U.S. Horticultural Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Orlando, Florida 32803-1419.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Floride</region></placeName><wicri:cityArea>U.S. Horticultural Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Orlando</wicri:cityArea></affiliation></author><author><name sortKey="Shapiro, J P" sort="Shapiro, J P" uniqKey="Shapiro J" first="J P" last="Shapiro">J P Shapiro</name></author><author><name sortKey="Doostdar, H" sort="Doostdar, H" uniqKey="Doostdar H" first="H" last="Doostdar">H. Doostdar</name></author><author><name sortKey="Mcdonald, R E" sort="Mcdonald, R E" uniqKey="Mcdonald R" first="R E" last="Mcdonald">R E Mcdonald</name></author><author><name sortKey="Niedz, R P" sort="Niedz, R P" uniqKey="Niedz R" first="R P" last="Niedz">R P Niedz</name></author><author><name sortKey="Nairn, C J" sort="Nairn, C J" uniqKey="Nairn C" first="C J" last="Nairn">C J Nairn</name></author><author><name sortKey="Hearn, C J" sort="Hearn, C J" uniqKey="Hearn C" first="C J" last="Hearn">C J Hearn</name></author><author><name sortKey="Mayer, R T" sort="Mayer, R T" uniqKey="Mayer R" first="R T" last="Mayer">R T Mayer</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:7952962</idno><idno type="pmid">7952962</idno><idno type="wicri:Area/PubMed/Corpus">000F45</idno><idno type="wicri:Area/PubMed/Curation">000F45</idno><idno type="wicri:Area/PubMed/Checkpoint">000F45</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identification and characterization of acidic hydrolases with chitinase and chitosanase activities from sweet orange callus tissue.</title><author><name sortKey="Osswald, W F" sort="Osswald, W F" uniqKey="Osswald W" first="W F" last="Osswald">W F Osswald</name><affiliation wicri:level="2"><nlm:affiliation>U.S. Horticultural Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Orlando, Florida 32803-1419.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Floride</region></placeName><wicri:cityArea>U.S. Horticultural Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Orlando</wicri:cityArea></affiliation></author><author><name sortKey="Shapiro, J P" sort="Shapiro, J P" uniqKey="Shapiro J" first="J P" last="Shapiro">J P Shapiro</name></author><author><name sortKey="Doostdar, H" sort="Doostdar, H" uniqKey="Doostdar H" first="H" last="Doostdar">H. Doostdar</name></author><author><name sortKey="Mcdonald, R E" sort="Mcdonald, R E" uniqKey="Mcdonald R" first="R E" last="Mcdonald">R E Mcdonald</name></author><author><name sortKey="Niedz, R P" sort="Niedz, R P" uniqKey="Niedz R" first="R P" last="Niedz">R P Niedz</name></author><author><name sortKey="Nairn, C J" sort="Nairn, C J" uniqKey="Nairn C" first="C J" last="Nairn">C J Nairn</name></author><author><name sortKey="Hearn, C J" sort="Hearn, C J" uniqKey="Hearn C" first="C J" last="Hearn">C J Hearn</name></author><author><name sortKey="Mayer, R T" sort="Mayer, R T" uniqKey="Mayer R" first="R T" last="Mayer">R T Mayer</name></author></analytic><series><title level="j">Plant & cell physiology</title><idno type="ISSN">0032-0781</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Chitinase (genetics)</term><term>Chitinase (isolation & purification)</term><term>Citrus (enzymology)</term><term>Citrus (genetics)</term><term>Glycoside Hydrolases (genetics)</term><term>Glycoside Hydrolases (isolation & purification)</term><term>Isoelectric Point</term><term>Molecular Sequence Data</term><term>Molecular Weight</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Chitinase</term><term>Glycoside Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Chitinase</term><term>Glycoside Hydrolases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Citrus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Citrus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Isoelectric Point</term><term>Molecular Sequence Data</term><term>Molecular Weight</term><term>Sequence Homology, Amino Acid</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Acidic chitinases (EC 3.2.1.14) were isolated and characterized from 4-week-old nonembryogenic Citrus sinensis L. Osbeck cv 'Valencia' callus tissue. The enzymes were purified using size exclusion, anion exchange, and chromatofocusing HPLC techniques. Eleven isoforms were isolated with M(r)s between 26,000 and 37,400. Eight of the isoforms were purified to homogeneity, and all but one cross-reacted with a polyclonal antibody raised against a basic class I potato leaf chitinase. The isoelectric points (determined by chromatofocusing) were from pH 4.5 to 5.4. All hydrolases degraded chitin and four were capable of hydrolyzing solubilized shrimp shell chitosan suggesting they may be chitosanases (EC 3.2.1.99). Apparent chitosanase activity generally decreased with decreasing acetylation of the chitosan (i.e. from 20% to 0% acetylation). The chitinases and chitinases/chitosanases are predominantly endochitinases. Chitosanase activity was optimal at pH 5 while the pH optimum for chitinase activity ranged between pH 3.5 and 5.5. The chitinases and chitinases/chitosanases were stable up to 60 degrees C and showed their highest enzyme activity at that temperature. N-terminal sequences were obtained on three of the isoforms. One of the isoforms was identified as a class II chitinase and the other two as class III chitinases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7952962</PMID><DateCreated><Year>1994</Year><Month>12</Month><Day>7</Day></DateCreated><DateCompleted><Year>1994</Year><Month>12</Month><Day>07</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0781</ISSN><JournalIssue CitedMedium="Print"><Volume>35</Volume><Issue>5</Issue><PubDate><Year>1994</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Plant & cell physiology</Title><ISOAbbreviation>Plant Cell Physiol.</ISOAbbreviation></Journal><ArticleTitle>Identification and characterization of acidic hydrolases with chitinase and chitosanase activities from sweet orange callus tissue.</ArticleTitle><Pagination><MedlinePgn>811-20</MedlinePgn></Pagination><Abstract><AbstractText>Acidic chitinases (EC 3.2.1.14) were isolated and characterized from 4-week-old nonembryogenic Citrus sinensis L. Osbeck cv 'Valencia' callus tissue. The enzymes were purified using size exclusion, anion exchange, and chromatofocusing HPLC techniques. Eleven isoforms were isolated with M(r)s between 26,000 and 37,400. Eight of the isoforms were purified to homogeneity, and all but one cross-reacted with a polyclonal antibody raised against a basic class I potato leaf chitinase. The isoelectric points (determined by chromatofocusing) were from pH 4.5 to 5.4. All hydrolases degraded chitin and four were capable of hydrolyzing solubilized shrimp shell chitosan suggesting they may be chitosanases (EC 3.2.1.99). Apparent chitosanase activity generally decreased with decreasing acetylation of the chitosan (i.e. from 20% to 0% acetylation). The chitinases and chitinases/chitosanases are predominantly endochitinases. Chitosanase activity was optimal at pH 5 while the pH optimum for chitinase activity ranged between pH 3.5 and 5.5. The chitinases and chitinases/chitosanases were stable up to 60 degrees C and showed their highest enzyme activity at that temperature. N-terminal sequences were obtained on three of the isoforms. One of the isoforms was identified as a class II chitinase and the other two as class III chitinases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Osswald</LastName><ForeName>W F</ForeName><Initials>WF</Initials><AffiliationInfo><Affiliation>U.S. Horticultural Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Orlando, Florida 32803-1419.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shapiro</LastName><ForeName>J P</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Doostdar</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>McDonald</LastName><ForeName>R E</ForeName><Initials>RE</Initials></Author><Author ValidYN="Y"><LastName>Niedz</LastName><ForeName>R P</ForeName><Initials>RP</Initials></Author><Author ValidYN="Y"><LastName>Nairn</LastName><ForeName>C J</ForeName><Initials>CJ</Initials></Author><Author ValidYN="Y"><LastName>Hearn</LastName><ForeName>C J</ForeName><Initials>CJ</Initials></Author><Author ValidYN="Y"><LastName>Mayer</LastName><ForeName>R T</ForeName><Initials>RT</Initials></Author></AuthorList><Language>ENG</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Japan</Country><MedlineTA>Plant Cell Physiol</MedlineTA><NlmUniqueID>9430925</NlmUniqueID><ISSNLinking>0032-0781</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D006026">Glycoside Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.132</RegistryNumber><NameOfSubstance UI="C019868">chitosanase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.14</RegistryNumber><NameOfSubstance UI="D002688">Chitinase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002688" MajorTopicYN="N">Chitinase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002957" MajorTopicYN="N">Citrus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007526" MajorTopicYN="N">Isoelectric Point</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>7</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7952962</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Floride</li></region></list><tree><noCountry><name sortKey="Doostdar, H" sort="Doostdar, H" uniqKey="Doostdar H" first="H" last="Doostdar">H. Doostdar</name><name sortKey="Hearn, C J" sort="Hearn, C J" uniqKey="Hearn C" first="C J" last="Hearn">C J Hearn</name><name sortKey="Mayer, R T" sort="Mayer, R T" uniqKey="Mayer R" first="R T" last="Mayer">R T Mayer</name><name sortKey="Mcdonald, R E" sort="Mcdonald, R E" uniqKey="Mcdonald R" first="R E" last="Mcdonald">R E Mcdonald</name><name sortKey="Nairn, C J" sort="Nairn, C J" uniqKey="Nairn C" first="C J" last="Nairn">C J Nairn</name><name sortKey="Niedz, R P" sort="Niedz, R P" uniqKey="Niedz R" first="R P" last="Niedz">R P Niedz</name><name sortKey="Shapiro, J P" sort="Shapiro, J P" uniqKey="Shapiro J" first="J P" last="Shapiro">J P Shapiro</name></noCountry><country name="États-Unis"><region name="Floride"><name sortKey="Osswald, W F" sort="Osswald, W F" uniqKey="Osswald W" first="W F" last="Osswald">W F Osswald</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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